DOI: 10.1083/jcb.141.6.1433. Differential Nuclear Translocation and Transactivation Potential of β-Catenin and Plakoglobin

Differential Nuclear Translocation and Transactivation Potential of β-Catenin and Plakoglobin

10.1083/jcb.141.6.1433

Crossref journal-article

Rockefeller University Press

The Journal of Cell Biology (291)

Abstract

β-Catenin and plakoglobin are homologous proteins that function in cell adhesion by linking cadherins to the cytoskeleton and in signaling by transactivation together with lymphoid-enhancing binding/T cell (LEF/TCF) transcription factors. Here we compared the nuclear translocation and transactivation abilities of β-catenin and plakoglobin in mammalian cells. Overexpression of each of the two proteins in MDCK cells resulted in nuclear translocation and formation of nuclear aggregates. The β-catenin-containing nuclear structures also contained LEF-1 and vinculin, while plakoglobin was inefficient in recruiting these molecules, suggesting that its interaction with LEF-1 and vinculin is significantly weaker. Moreover, transfection of LEF-1 translocated endogenous β-catenin, but not plakoglobin to the nucleus. Chimeras consisting of Gal4 DNA-binding domain and the transactivation domains of either plakoglobin or β-catenin were equally potent in transactivating a Gal4-responsive reporter, whereas activation of LEF-1– responsive transcription was significantly higher with β-catenin. Overexpression of wild-type plakoglobin or mutant β-catenin lacking the transactivation domain induced accumulation of the endogenous β-catenin in the nucleus and LEF-1–responsive transactivation. It is further shown that the constitutive β-catenin–dependent transactivation in SW480 colon carcinoma cells and its nuclear localization can be inhibited by overexpressing N-cadherin or α-catenin. The results indicate that (a) plakoglobin and β-catenin differ in their nuclear translocation and complexing with LEF-1 and vinculin; (b) LEF-1–dependent transactivation is preferentially driven by β-catenin; and (c) the cytoplasmic partners of β-catenin, cadherin and α-catenin, can sequester it to the cytoplasm and inhibit its transcriptional activity.

Bibliography

Simcha, I., Shtutman, M., Salomon, D., Zhurinsky, J., Sadot, E., Geiger, B., & Ben-Zeâev, A. (1998). Differential Nuclear Translocation and Transactivation Potential of Î²-Catenin and Plakoglobin. The Journal of Cell Biology, 141(6), 1433â1448.

Authors 7

Inbal Simcha (first)
Michael Shtutman (additional)
Daniela Salomon (additional)
Jacob Zhurinsky (additional)
Einat Sadot (additional)
Benjamin Geiger (additional)
Avri Ben-Ze'ev (additional)

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Dates

Type	When
Created	23 years, 1 month ago (July 26, 2002, 12:47 p.m.)
Deposited	2 years, 1 month ago (July 22, 2023, 3:47 a.m.)
Indexed	2 months, 1 week ago (June 26, 2025, 2:24 p.m.)
Issued	27 years, 2 months ago (June 15, 1998)
Published	27 years, 2 months ago (June 15, 1998)
Published Online	27 years, 2 months ago (June 15, 1998)
Published Print	27 years, 2 months ago (June 15, 1998)

Funders 0

None

BibTeX

@article{Simcha_1998, title={Differential Nuclear Translocation and Transactivation Potential of β-Catenin and Plakoglobin}, volume={141}, ISSN={1540-8140}, url={http://dx.doi.org/10.1083/jcb.141.6.1433}, DOI={10.1083/jcb.141.6.1433}, number={6}, journal={The Journal of Cell Biology}, publisher={Rockefeller University Press}, author={Simcha, Inbal and Shtutman, Michael and Salomon, Daniela and Zhurinsky, Jacob and Sadot, Einat and Geiger, Benjamin and Ben-Ze’ev, Avri}, year={1998}, month=jun, pages={1433–1448} }

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  "abstract": "<jats:p>\u03b2-Catenin and plakoglobin are homologous proteins that function in cell adhesion by linking cadherins to the cytoskeleton and in signaling by transactivation together with lymphoid-enhancing binding/T cell (LEF/TCF) transcription factors. Here we compared the nuclear translocation and transactivation abilities of \u03b2-catenin and plakoglobin in mammalian cells. Overexpression of each of the two proteins in MDCK cells resulted in nuclear translocation and formation of nuclear aggregates. The \u03b2-catenin-containing nuclear structures also contained LEF-1 and vinculin, while plakoglobin was inefficient in recruiting these molecules, suggesting that its interaction with LEF-1 and vinculin is significantly weaker. Moreover, transfection of LEF-1 translocated endogenous \u03b2-catenin, but not plakoglobin to the nucleus. Chimeras consisting of Gal4 DNA-binding domain and the transactivation domains of either plakoglobin or \u03b2-catenin were equally potent in transactivating a Gal4-responsive reporter, whereas activation of LEF-1\u2013 responsive transcription was significantly higher with \u03b2-catenin. Overexpression of wild-type plakoglobin or mutant \u03b2-catenin lacking the transactivation domain induced accumulation of the endogenous \u03b2-catenin in the nucleus and LEF-1\u2013responsive transactivation. It is further shown that the constitutive \u03b2-catenin\u2013dependent transactivation in SW480 colon carcinoma cells and its nuclear localization can be inhibited by overexpressing N-cadherin or \u03b1-catenin. The results indicate that (a) plakoglobin and \u03b2-catenin differ in their nuclear translocation and complexing with LEF-1 and vinculin; (b) LEF-1\u2013dependent transactivation is preferentially driven by \u03b2-catenin; and (c) the cytoplasmic partners of \u03b2-catenin, cadherin and \u03b1-catenin, can sequester it to the cytoplasm and inhibit its transcriptional activity.</jats:p>",
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